ID A0A2I3SUM8_PANTR Unreviewed; 230 AA.
AC A0A2I3SUM8; A0A2J8QK56;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Thiamine-triphosphatase {ECO:0000256|ARBA:ARBA00020088, ECO:0000256|PIRNR:PIRNR036561};
DE Short=ThTPase {ECO:0000256|PIRNR:PIRNR036561};
DE EC=3.6.1.28 {ECO:0000256|ARBA:ARBA00012378, ECO:0000256|PIRNR:PIRNR036561};
GN Name=THTPA {ECO:0000313|EMBL:JAA08925.1,
GN ECO:0000313|Ensembl:ENSPTRP00000080699.1,
GN ECO:0000313|VGNC:VGNC:12471};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000080699.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000080699.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA08925.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA08925.1}, Skin
RC {ECO:0000313|EMBL:JAA26258.1}, and Smooth vascular
RC {ECO:0000313|EMBL:JAA14952.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000080699.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CC {ECO:0000256|ARBA:ARBA00002106, ECO:0000256|PIRNR:PIRNR036561}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + thiamine triphosphate = H(+) + phosphate + thiamine
CC diphosphate; Xref=Rhea:RHEA:11744, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58937,
CC ChEBI:CHEBI:58938; EC=3.6.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00000052,
CC ECO:0000256|PIRNR:PIRNR036561};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR036561-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR036561-2};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|PIRNR:PIRNR036561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR036561}.
CC -!- SIMILARITY: Belongs to the ThTPase family.
CC {ECO:0000256|ARBA:ARBA00008181, ECO:0000256|PIRNR:PIRNR036561}.
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DR EMBL; AACZ04059395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01002413; JAA08925.1; -; mRNA.
DR EMBL; GABC01002412; JAA08926.1; -; mRNA.
DR EMBL; GABF01007193; JAA14952.1; -; mRNA.
DR EMBL; GABD01006842; JAA26258.1; -; mRNA.
DR EMBL; GABD01006841; JAA26259.1; -; mRNA.
DR RefSeq; XP_009425806.1; XM_009427531.2.
DR RefSeq; XP_009425807.1; XM_009427532.2.
DR RefSeq; XP_016781393.1; XM_016925904.1.
DR STRING; 9598.ENSPTRP00000080699; -.
DR PaxDb; 9598-ENSPTRP00000010488; -.
DR Ensembl; ENSPTRT00000101932.1; ENSPTRP00000080699.1; ENSPTRG00000006180.5.
DR GeneID; 745282; -.
DR KEGG; ptr:745282; -.
DR CTD; 79178; -.
DR VGNC; VGNC:12471; THTPA.
DR GeneTree; ENSGT00390000005996; -.
DR OMA; HWLRHRE; -.
DR OrthoDB; 5489660at2759; -.
DR TreeFam; TF333398; -.
DR Proteomes; UP000002277; Chromosome 14.
DR Bgee; ENSPTRG00000006180; Expressed in prefrontal cortex and 21 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0050333; F:thiamine triphosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0042357; P:thiamine diphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07758; ThTPase; 1.
DR Gene3D; 2.40.320.10; Hypothetical Protein Pfu-838710-001; 1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR039582; THTPA.
DR InterPro; IPR012177; ThTPase_euk.
DR PANTHER; PTHR14586; THIAMINE-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR14586:SF1; THIAMINE-TRIPHOSPHATASE; 1.
DR Pfam; PF01928; CYTH; 1.
DR PIRSF; PIRSF036561; ThTPase; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; CYTH-like phosphatases; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR036561};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036561};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036561-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036561-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT DOMAIN 5..201
FT /note="CYTH"
FT /evidence="ECO:0000259|PROSITE:PS51707"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
SQ SEQUENCE 230 AA; 25557 MW; 69D5ADFBE8EEA4A2 CRC64;
MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTSELSLMQA DHWLRRREDS
GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLGADG LGAGDVAAVL GPLGLQEVAS
FVTKRSAWKL VLLEADEEEP QLRVDLDTAD FGYVVGEVEA LVHEEAEVPT ALEKIHRLSS
MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG
//